Heterologous expression, characterization and structural studies of a hydrophobic peptide from the HIV-1 p24 protein

• Published in: Peptides (New York, N.Y. : 1980) Vol. 26; no. 2; pp. 243 - 249
• Main Authors: Castilho, Priscila V., Campana, Patricia T., Garcia, Assuero F., Beltramini, Leila M., Araújo, Ana Paula U.
• Format: Journal Article
• Language: English
• Published: New York, NY Elsevier Inc 01.02.2005; Elsevier Science
• Subjects: Biological and medical sciences; Circular Dichroism; Escherichia coli - genetics; Fluorescence spectroscopy; Fundamental and applied biological sciences. Psychology; Genetic Vectors; HIV Core Protein p24 - chemistry; Hydrophobic and Hydrophilic Interactions; Mass Spectrometry; p24 HIV-1; Peptides - chemistry; Peptides - genetics; Peptides - metabolism; Protein Structure, Secondary; Recombinant Fusion Proteins - chemistry; Recombinant Fusion Proteins - metabolism; Recombinant peptide; Sequence Analysis, Protein; Solubility; Spectrometry, Fluorescence; Synthetic gene; Vertebrates: endocrinology; Fluorescence spectroscopy; Recombinant peptide; IPTG; p24 HIV-1; rp24-3m; Trx; ɛ; Synthetic gene; rp24-3; Circular dichroism; Peptides; Retroviridae; Fluorescence; Lentivirus; Protein; Virus; Characterization; Gene; Human immunodeficiency virus

Proteins from the inner core of HIV-1, such as the capsid protein (p24), are involved in crucial processes during the virus life cycle. The p24 protein plays an active structural role in the Gag protein and in its mature form. This work describes the production of a peptide derived from the p24 C-te...